Interaction of catalase with carrageenan applied to its recovery from murine liver

Galante, Micaela; Belluzo, Soledad; Picó, Guillermo; Boeris, Valeria

doi:10.1016/j.seppur.2013.03.027

Cited by 3 publications

(1 citation statement)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, the formation of inter- and intrachain complexes between proteins and polymers prior to coacervation is readily seen in PE–protein systems, but such precursors have been less evident for HP coacervation. Different equilibria in the latter case might explain the appearance of coacervates ,, rather than the precipitates more commonly encountered in the use of polyelectrolytes for protein purification. − In this study we seek (1) to characterize the molecular processes that lead to LLPS in HP systems, analogous to those surmised for PE–protein coacervation, and (2) to expand the current model for HP coacervates by relating the conditions required for coacervation to equilibria among complexes and free proteins.…”

Section: Introductionmentioning

confidence: 99%

Complex Equilibria, Speciation, and Heteroprotein Coacervation of Lactoferrin and β-Lactoglobulin

et al. 2015

View full text Add to dashboard Cite

There has been a resurgence of interest in complex coacervation, a form of liquid-liquid phase separation (LLPS) in systems of oppositely charged macroions, but very few reports describe the somewhat anomalous coacervation between acidic and basic proteins, which occurs under very narrow ranges of conditions. We sought to identify the roles of equilibrium interprotein complexes during the coacervation of β-lactoglobulin dimer (BLG2) with lactoferrin (LF) and found that this LLPS arises specifically from LF(BLG2)2. We followed the progress of complexation and coacervation as a function of r, the LF/BLG molar ratio, using turbidity to monitor the degree of coacervation and proton release and dynamic light scattering (DLS) to assess the stoichiometry and abundance of complexes. Isothermal titration calorimetry (ITC) showed that initial complex formation is endothermic, but a large exotherm related to coacervate formation obscured other regions. On the basis of turbidimetry, proton release, and DLS, we propose a speciation diagram that presents the abundance of various complexes as a function of r. Although multiple species could be simultaneously present, distinct regions could be identified corresponding to equilibria among particular protein pairs.

show abstract